Evidence map›Paper›PMID 32751900›Full record

ArticleBiomolecules2020

Structural Characterization of an

Timo Meyer, Nadine Zumbrägel, Christina Geerds, Harald Gröger, Hartmut H Niemann

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.6field-weighted citation impact, top 35% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB.Acta crystallographica. Section F, Structural biology communications · 2021
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Timo MeyerStructural Biochemistry, Faculty of Chemistry, Bielefeld University, Universitätsstraße 25, 33615 Bielefeld, Germany.
Nadine ZumbrägelIndustrial Organic Chemistry and Biotechnology, Faculty of Chemistry, Bielefeld University, Universitätsstraße 25, 33615 Bielefeld, Germany.ORCID 0000-0002-3493-8852
Christina GeerdsStructural Biochemistry, Faculty of Chemistry, Bielefeld University, Universitätsstraße 25, 33615 Bielefeld, Germany.
Harald GrögerIndustrial Organic Chemistry and Biotechnology, Faculty of Chemistry, Bielefeld University, Universitätsstraße 25, 33615 Bielefeld, Germany.ORCID 0000-0001-8582-2107
Hartmut H NiemannStructural Biochemistry, Faculty of Chemistry, Bielefeld University, Universitätsstraße 25, 33615 Bielefeld, Germany.ORCID 0000-0002-8582-0360
Bielefeld University · DE

Funding

Bundesministerium für Bildung und Forschung 031A184AHelmholtz-Zentrum Berlin für Materialien und Energie BESSY 2: 169
6 · The paper itself

Abstract

NADPH-dependent imine reductases (IREDs) are enzymes capable of enantioselectively reducing imines to chiral secondary amines, which represent important building blocks in the chemical and pharmaceutical industry. Since their discovery in 2011, many previously unknown IREDs have been identified, biochemically and structurally characterized and categorized into families. However, the catalytic mechanism and guiding principles for substrate specificity and stereoselectivity remain disputed. Herein, we describe the crystal structure of

Indexed as

Bacterial ProteinsCatalytic DomainIminesMycobacterium smegmatisNADPOxidoreductasesProtein BindingStereoisomerismSubstrate SpecificityBacterial ProteinsIminesNADPOxidoreductases2-ethylhexanolbiocatalysiscrystal structureenzymeimine reductasesubstrate bindingsubstrate soaking

Identifiers

PMID32751900
PMCPMC7465668
OpenAlexW3046912696

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.